Transglycosylation activity of cellobiohydrolase I from Trichoderma longibrachiatum on synthetic and natural substrates
Using 4-methylumbelliferyl (MUF) ß- d-cellobioside as a substrate, the ability of cellobiohydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In...
Saved in:
Published in | Biochimica et biophysica acta Vol. 1073; no. 3; pp. 481 - 485 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
09.04.1991
Elsevier |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Using 4-methylumbelliferyl (MUF) ß-
d-cellobioside as a substrate, the ability of cellobiohydrolase I from
Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In the course of enzymatic reaction, a concentration of the transglycosylation product passed through a maximum, since at later stages of the reaction the product was further hydrolyzed. At MUF-ß-
d-cellobioside concentrations of 2–10 mM, the maximum weight content of MUF-tetrasaccharide amounted to 1–4% of the total content of saccharides. In the reaction system, containing 2.5 mM MUF-ß-
d-cellobioside and 10 mM MUF-ß-
d-glucoside MUF-trisaccharide was formed as the main transglycosylation product. In hydrolysis of natural substrates (cellulose and cellotriose) in the presence of MUF-ß-
d-glucoside a formation of MUF-trisaccharide was also observed. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0304-4165 0006-3002 1872-8006 |
DOI: | 10.1016/0304-4165(91)90219-7 |